SCTN_PSESH
ID SCTN_PSESH Reviewed; 449 AA.
AC Q8RK01;
DT 15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Type 3 secretion system ATPase {ECO:0000305};
DE Short=T3SS ATPase {ECO:0000305};
DE EC=7.4.2.8 {ECO:0000305|PubMed:12734178};
GN Name=sctN {ECO:0000250|UniProtKB:Q52371};
GN Synonyms=hrcN {ECO:0000303|PubMed:12734178};
OS Pseudomonas savastanoi pv. phaseolicola (Pseudomonas syringae pv.
OS phaseolicola).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=319;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, ATPASE ACTIVITY, CATALYTIC
RP ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND
RP SUBCELLULAR LOCATION.
RX PubMed=12734178; DOI=10.1074/jbc.m301903200;
RA Pozidis C., Chalkiadaki A., Gomez-Serrano A., Stahlberg H., Brown I.,
RA Tampakaki A.P., Lustig A., Sianidis G., Politou A.S., Engel A.,
RA Panopoulos N.J., Mansfield J., Pugsley A.P., Karamanou S., Economou A.;
RT "Type III protein translocase: HrcN is a peripheral ATPase that is
RT activated by oligomerization.";
RL J. Biol. Chem. 278:25816-25824(2003).
RN [2]
RP SUBUNIT, AND CRYO-ELECTRON MICROSCOPY.
RX PubMed=16824099; DOI=10.1111/j.1365-2958.2006.05219.x;
RA Mueller S.A., Pozidis C., Stone R., Meesters C., Chami M., Engel A.,
RA Economou A., Stahlberg H.;
RT "Double hexameric ring assembly of the type III protein translocase ATPase
RT HrcN.";
RL Mol. Microbiol. 61:119-125(2006).
CC -!- FUNCTION: ATPase component of the type III secretion system (T3SS),
CC also called injectisome, which is used to inject bacterial effector
CC proteins into eukaryotic host cells (PubMed:12734178). Acts as a
CC molecular motor to provide the energy that is required for the export
CC of proteins (Probable). Required for type III secretion apparatus
CC (T3SA) formation, proper protein secretion, host cell invasion and
CC virulence (By similarity). May play a critical role in T3SS substrate
CC recognition, disassembly of the effector/chaperone complex and
CC unfolding of the effector in an ATP-dependent manner prior to secretion
CC (By similarity). {ECO:0000250|UniProtKB:P0A1B9,
CC ECO:0000250|UniProtKB:P0A1C1, ECO:0000269|PubMed:12734178,
CC ECO:0000305|PubMed:12734178}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + cellular proteinSide 1 = ADP + phosphate +
CC cellular proteinSide 2.; EC=7.4.2.8;
CC Evidence={ECO:0000305|PubMed:12734178};
CC -!- ACTIVITY REGULATION: Oligomerization increases ATPase activity.
CC {ECO:0000269|PubMed:12734178}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.3 mM for ATP (dodecameric form) {ECO:0000269|PubMed:12734178};
CC KM=0.114 mM for ATP (monomeric form) {ECO:0000269|PubMed:12734178};
CC Vmax=43 mmol/min/mg enzyme for ATPase activity (dodecameric form)
CC {ECO:0000269|PubMed:12734178};
CC Vmax=0.0635 mmol/min/mg enzyme for ATPase activity (monomeric form)
CC {ECO:0000269|PubMed:12734178};
CC -!- SUBUNIT: The core secretion machinery of the T3SS is composed of
CC approximately 20 different proteins, including cytoplasmic components,
CC a base, an export apparatus and a needle (By similarity). This subunit
CC is part of the cytosolic complex (PubMed:12734178). Forms
CC homododecamers (PubMed:12734178, PubMed:16824099). Comprises two
CC hexameric rings that are probably stacked face-to-face by the
CC association of their C-terminal domains (PubMed:16824099). Also present
CC as monomer and homohexamer in solution (PubMed:12734178).
CC {ECO:0000250|UniProtKB:Q52371, ECO:0000269|PubMed:12734178,
CC ECO:0000269|PubMed:16824099}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12734178}.
CC Note=Associates with the inner membrane. {ECO:0000269|PubMed:12734178}.
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family. T3SS ATPase
CC subfamily. {ECO:0000305}.
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DR EMBL; AJ430232; CAD22886.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8RK01; -.
DR SMR; Q8RK01; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0030257; C:type III protein secretion system complex; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0008564; F:protein-exporting ATPase activity; IEA:UniProtKB-EC.
DR GO; GO:0046034; P:ATP metabolic process; IEA:InterPro.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR GO; GO:0030254; P:protein secretion by the type III secretion system; IEA:InterPro.
DR GO; GO:1902600; P:proton transmembrane transport; IEA:InterPro.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR020003; ATPase_a/bsu_AS.
DR InterPro; IPR004100; ATPase_F1/V1/A1_a/bsu_N.
DR InterPro; IPR000194; ATPase_F1/V1/A1_a/bsu_nucl-bd.
DR InterPro; IPR005714; ATPase_T3SS_FliI/YscN.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR040627; T3SS_ATPase_C.
DR Pfam; PF00006; ATP-synt_ab; 1.
DR Pfam; PF02874; ATP-synt_ab_N; 1.
DR Pfam; PF18269; T3SS_ATPase_C; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR01026; fliI_yscN; 1.
DR PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Nucleotide-binding; Protein transport; Translocase;
KW Transport; Virulence.
FT CHAIN 1..449
FT /note="Type 3 secretion system ATPase"
FT /id="PRO_0000144701"
FT BINDING 178..183
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P0A1C1"
SQ SEQUENCE 449 AA; 48466 MW; 2DFAA6E4A08C843F CRC64;
MNAALSQWKD AHAARLRDYS AVRVSGRVSA VRGILLECKI PAAKVGDLCE VSKADGSFLL
AEIVGFTQEC TLLSALGAPD GIQVGAPIRP LGIAHRIGVD DSLLGCVLDG FGRPLLGDCL
GAFAGPDDRR ETLPVIADAL PPTQRPRITN ALPTGVRAID SAILLGEGQR VGLFAGAGCG
KTTLMAELAR NMGCDVIVFG LIGERGRELR EFLDHELDET LRRRSVLVCA TSDRSSMERA
RAAFTATAIA EAFRARGQKV LLLLDSLTRF ARAQREIGIA SGEPLGRGGL PPSVYTLLPR
LVERAGMSEN GSITALYTVL IEQDSMNDPV ADEVRSLLDG HIVLSRKLAE RGHYPAIDVS
ASISRILSNV TGREHQRANN RLRQLLAAYK QVEMLLRLGE YQAGADPVTD CAVQLNDDIN
EFLRQDLREP VPLQETLDGL LRLTSRLPE
